ID   COAX_PELTS              Reviewed;         256 AA.
AC   A5D5P9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Type III pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01274};
DE            EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01274};
DE   AltName: Full=PanK-III {ECO:0000255|HAMAP-Rule:MF_01274};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01274};
GN   Name=coaX {ECO:0000255|HAMAP-Rule:MF_01274}; OrderedLocusNames=PTH_0258;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC         H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         EC=2.7.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC   -!- COFACTOR:
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC       Note=A monovalent cation. Ammonium or potassium. {ECO:0000255|HAMAP-
CC       Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01274}.
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DR   EMBL; AP009389; BAF58439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D5P9; -.
DR   SMR; A5D5P9; -.
DR   STRING; 370438.PTH_0258; -.
DR   EnsemblBacteria; BAF58439; BAF58439; PTH_0258.
DR   KEGG; pth:PTH_0258; -.
DR   eggNOG; COG1521; Bacteria.
DR   HOGENOM; CLU_066627_1_0_9; -.
DR   OMA; HEPWLTL; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000006556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004619; Type_III_PanK.
DR   PANTHER; PTHR34265; PTHR34265; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR00671; baf; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; Metal-binding;
KW   Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT   CHAIN           1..256
FT                   /note="Type III pantothenate kinase"
FT                   /id="PRO_1000085856"
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         6..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         107..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         129
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
SQ   SEQUENCE   256 AA;  27736 MW;  024C746D6EB54085 CRC64;
     MILVFDVGNT NIVLGVFSGS RLVANWRLST DRYRTSDEYG IMLRELFAFS GLEMKQIKAV
     VVSTVVPPLT FTLERLCQKY FNLTPLVVGP GIKTGLSIKI DNPREVGADR IVNAVAGYEQ
     YGGPLVIVDF GTATTFCAVS ARGEYLGGAI APGISISTEA LFARAAKLPR VEVVKPLSVI
     GRNTVASMQA GIFYGFVGQV DEIVKRMKKE LGENTRVIAT GGLAGLIAQE SATIEQVDPF
     LTLKGLRLIY ERNAQR